Evidence map›Paper›PMID 20826699›Full record

ArticleRNA (New York, N.Y.)2010

Distinct functions of maternal and somatic Pat1 protein paralogs.

Aline Marnef, Maria Maldonado, Anthony Bugaut, Shankar Balasubramanian, Michel Kress, Dominique Weil, Nancy Standart

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Novel PATL2 variants cause female infertility with oocyte maturation defect.Journal of assisted reproduction and genetics · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Aline MarnefDepartment of Biochemistry, University of Cambridge, Cambridge CB21QW, United Kingdom.
Maria Maldonado
Anthony Bugaut
Shankar Balasubramanian
Michel Kress
Dominique Weil
Nancy Standart
University of Cambridge · GBCentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/E019773/1Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

We previously identified Xenopus Pat1a (P100) as a member of the maternal CPEB RNP complex, whose components resemble those of P-(rocessing) bodies, and which is implicated in translational control in Xenopus oocytes. Database searches have identified Pat1a proteins in other vertebrates, as well as paralogous Pat1b proteins. Here we characterize Pat1 proteins, which have no readily discernable sequence features, in Xenopus oocytes, eggs, and early embryos and in human tissue culture cells. xPat1a and 1b have essentially mutually exclusive expression patterns in oogenesis and embryogenesis. xPat1a is degraded during meiotic maturation, via PEST-like regions, while xPat1b mRNA is translationally activated at GVBD by cytoplasmic polyadenylation. Pat1 proteins bind RNA in vitro, via a central domain, with a preference for G-rich sequences, including the NRAS 5' UTR G-quadruplex-forming sequence. When tethered to reporter mRNA, both Pat proteins repress translation in oocytes. Indeed, both epitope-tagged proteins interact with the same components of the CPEB RNP complex, including CPEB, Xp54, eIF4E1b, Rap55B, and ePAB. However, examining endogenous protein interactions, we find that in oocytes only xPat1a is a bona fide component of the CPEB RNP, and that xPat1b resides in a separate large complex. In tissue culture cells, hPat1b localizes to P-bodies, while mPat1a-GFP is either found weakly in P-bodies or disperses P-bodies in a dominant-negative fashion. Altogether we conclude that Pat1a and Pat1b proteins have distinct functions, mediated in separate complexes. Pat1a is a translational repressor in oocytes in a CPEB-containing complex, and Pat1b is a component of P-bodies in somatic cells.

Indexed as

AnimalsBase SequenceCell LineDNA-Binding ProteinsFemaleHumansMiceOocytesPhylogenyProtein BindingProtein BiosynthesisRNARNA-Binding ProteinsRNA, MessengerXenopus laevisXenopus ProteinsDNA-Binding ProteinsPATL1 protein, humanPATL1 protein, XenopusPATL2 protein, XenopusRNARNA-Binding ProteinsRNA, MessengerXenopus Proteins

Identifiers

PMID20826699
PMCPMC2957050
OpenAlexW2106260355

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.